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1NDD

STRUCTURE OF NEDD8

1NDD の概要
エントリーDOI10.2210/pdb1ndd/pdb
分子名称PROTEIN (UBIQUITIN-LIKE PROTEIN NEDD8), CHLORIDE ION, SULFATE ION, ... (4 entities in total)
機能のキーワードnedd8, nedd-8, ubiquitin-like, proteolysis, signaling protein
由来する生物種Homo sapiens (human)
細胞内の位置Nucleus: Q15843
タンパク質・核酸の鎖数4
化学式量合計34751.07
構造登録者
Whitby, F.G.,Xia, G.,Pickart, C.M.,Hill, C.P. (登録日: 1998-08-21, 公開日: 1999-02-23, 最終更新日: 2023-08-16)
主引用文献Whitby, F.G.,Xia, G.,Pickart, C.M.,Hill, C.P.
Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes.
J.Biol.Chem., 273:34983-34991, 1998
Cited by
PubMed Abstract: The NEDD8/Rub1 class of ubiquitin-like proteins has been implicated in progression of the cell cycle from G1 into S phase. These molecules undergo a metabolism that parallels that of ubiquitin and involves specific interactions with many different proteins. We report here the crystal structure of recombinant human NEDD8 refined at 1.6-A resolution to an R factor of 21.9%. As expected from the high sequence similarity (57% identical), the NEDD8 structure closely resembles that reported previously for ubiquitin. We also show that recombinant human NEDD8 protein is activated, albeit inefficiently, by the ubiquitin-activating (E1) enzyme and that NEDD8 can be transferred from E1 to the ubiquitin conjugating enzyme E2-25K. E2-25K adds NEDD8 to a polyubiquitin chain with an efficiency similar to that of ubiquitin. A chimeric tetramer composed of three ubiquitins and one histidine-tagged NEDD8 binds to the 26 S proteasome with an affinity similar to that of tetraubiquitin. Seven residues that differ from the corresponding residues in ubiquitin, but are conserved between NEDD8 orthologs, are candidates for mediating interactions with NEDD8-specific partners. One such residue, Ala-72 (Arg in ubiquitin), is shown to perform a key role in selecting against reaction with the ubiquitin E1 enzyme, thereby acting to prevent the inappropriate diversion of NEDD8 into ubiquitin-specific pathways.
PubMed: 9857030
DOI: 10.1074/jbc.273.52.34983
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.6 Å)
構造検証レポート
Validation report summary of 1ndd
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-03-04に公開中

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